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cell+culture+flasks
Numéro de catalogue:
(BOSSBS-6560R-A488)
Fournisseur:
Bioss
Description:
The Oxysterol-binding protein (OSBP) family of proteins consist of OSBP (OSBP1) and OSBP2 (ORP-4), which share a high overall similarity. OSBPs are involved in lipid metabolism and signal transduction, as well as vesicle transport, and can translocate to the periphery of Golgi membranes when they are bound to oxysterols. The OSBP protein transports sterols from lysosomes to the nucleus, where sterols downregulate the genes for HMG synthetase, HMG-CoA reductase and the low density lipoprotein receptor (LDLR). OSBP localizes to the cytosol and is widely expressed, while OSBP2 is mainly detected in testis, retina and fetal liver. The extracellular signal-regulated kinase (ERK) signaling pathway is controlled by OSBP via its cholesterol-binding properties. OSBP binds with a high affinity to 25-hydroxy-cholesterol (25-HC), a suppressor of cholesterol synthesis gene transcription in cultured cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13597R-A680)
Fournisseur:
Bioss
Description:
The homeobox protein, HESX1, which is also known as Rathke?s pouch homeobox, HANF, homeodomain transcription factor, and anterior-restricted homeobox protein is a transcription factor that belongs to the homeodomain family of DNA binding proteins. HESX1 is initially expressed in embryonic stem cells and the primitive forebrain, and is essential for normal development of the eyes and other anterior CNS structures, such as the hypothalamus, the pituitary gland and the olfactory bulbs. The homeobox gene Hesx1 is expressed in the anterior visceral endoderm (AVE), anterior axial mesendoderm (AME), and anterior neural ectoderm (ANE) during early embryogenesis. Mutations in the Hesx1 gene are associated with disorders that are comparable with septo-optic dysplasia (SOD). These disorders are characterized by hypoplasia of the optic nerve, various types of forebrain defects and pituitary hormone deficiencies, including hypothyroidism. Hesx1 also acts as a transcriptional repressor of reporter gene constructs in tissue culture assays.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11955R-A555)
Fournisseur:
Bioss
Description:
SLITRK family proteins are integral membrane proteins that have a C-terminal domain that is partially similar to TRK neurotrophin receptor proteins and two leucine-rich repeat (LRR) domains that are similar to those of SLIT proteins. SLITRK2 (SLIT and NTRK-like protein 2) is a 845 amino acid single-pass type I membrane protein that contains 14 LRR (leucine-rich) repeats and is expressed in neural tissues, with highest levels found in adult cerebral cortex. Overexpression of SLITRK2 leads to inhibition of unipolar neurites in cultured cells, suggesting that it suppresses neurite outgrowth. Inhibitory activity of SLITRK2 is localized to its C-terminal intracellular domain and without this region the protein induces neurite outgrowth. Variants in the gene encoding SLITRK2 may contribute to the development of bipolar disorder, autism spectrum disorder and schizophrenia. There are two isoforms of SLITRK2 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11955R-A350)
Fournisseur:
Bioss
Description:
SLITRK family proteins are integral membrane proteins that have a C-terminal domain that is partially similar to TRK neurotrophin receptor proteins and two leucine-rich repeat (LRR) domains that are similar to those of SLIT proteins. SLITRK2 (SLIT and NTRK-like protein 2) is a 845 amino acid single-pass type I membrane protein that contains 14 LRR (leucine-rich) repeats and is expressed in neural tissues, with highest levels found in adult cerebral cortex. Overexpression of SLITRK2 leads to inhibition of unipolar neurites in cultured cells, suggesting that it suppresses neurite outgrowth. Inhibitory activity of SLITRK2 is localized to its C-terminal intracellular domain and without this region the protein induces neurite outgrowth. Variants in the gene encoding SLITRK2 may contribute to the development of bipolar disorder, autism spectrum disorder and schizophrenia. There are two isoforms of SLITRK2 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11955R-A488)
Fournisseur:
Bioss
Description:
SLITRK family proteins are integral membrane proteins that have a C-terminal domain that is partially similar to TRK neurotrophin receptor proteins and two leucine-rich repeat (LRR) domains that are similar to those of SLIT proteins. SLITRK2 (SLIT and NTRK-like protein 2) is a 845 amino acid single-pass type I membrane protein that contains 14 LRR (leucine-rich) repeats and is expressed in neural tissues, with highest levels found in adult cerebral cortex. Overexpression of SLITRK2 leads to inhibition of unipolar neurites in cultured cells, suggesting that it suppresses neurite outgrowth. Inhibitory activity of SLITRK2 is localized to its C-terminal intracellular domain and without this region the protein induces neurite outgrowth. Variants in the gene encoding SLITRK2 may contribute to the development of bipolar disorder, autism spectrum disorder and schizophrenia. There are two isoforms of SLITRK2 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
This MAb recognizes human 17-26 kDa protein, which is identified as cytokine TNF-alpha (Tumor Necrosis Factor-alpha). TNF-alpha can be expressed as a 17 kDa free molecule, or as a 26 kDa membrane protein. TNF-alpha is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production. TNF alpha is currently being evaluated in treatment of certain cancers and AIDS Related Complex.
Fournisseur:
STEMBIOSYS
Description:
CELLvo™ human mesenchymal stem cells-Wharton's Jelly are adult multipotent stem cells cryopreserved at passage two.
Numéro de catalogue:
(BOSSBS-11988R-A350)
Fournisseur:
Bioss
Description:
Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11988R-FITC)
Fournisseur:
Bioss
Description:
Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11988R-HRP)
Fournisseur:
Bioss
Description:
Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11988R-CY5)
Fournisseur:
Bioss
Description:
Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6560R-A647)
Fournisseur:
Bioss
Description:
The Oxysterol-binding protein (OSBP) family of proteins consist of OSBP (OSBP1) and OSBP2 (ORP-4), which share a high overall similarity. OSBPs are involved in lipid metabolism and signal transduction, as well as vesicle transport, and can translocate to the periphery of Golgi membranes when they are bound to oxysterols. The OSBP protein transports sterols from lysosomes to the nucleus, where sterols downregulate the genes for HMG synthetase, HMG-CoA reductase and the low density lipoprotein receptor (LDLR). OSBP localizes to the cytosol and is widely expressed, while OSBP2 is mainly detected in testis, retina and fetal liver. The extracellular signal-regulated kinase (ERK) signaling pathway is controlled by OSBP via its cholesterol-binding properties. OSBP binds with a high affinity to 25-hydroxy-cholesterol (25-HC), a suppressor of cholesterol synthesis gene transcription in cultured cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13597R-CY5)
Fournisseur:
Bioss
Description:
The homeobox protein, HESX1, which is also known as Rathke’s pouch homeobox, HANF, homeodomain transcription factor, and anterior-restricted homeobox protein is a transcription factor that belongs to the homeodomain family of DNA binding proteins. HESX1 is initially expressed in embryonic stem cells and the primitive forebrain, and is essential for normal development of the eyes and other anterior CNS structures, such as the hypothalamus, the pituitary gland and the olfactory bulbs. The homeobox gene Hesx1 is expressed in the anterior visceral endoderm (AVE), anterior axial mesendoderm (AME), and anterior neural ectoderm (ANE) during early embryogenesis. Mutations in the Hesx1 gene are associated with disorders that are comparable with septo-optic dysplasia (SOD). These disorders are characterized by hypoplasia of the optic nerve, various types of forebrain defects and pituitary hormone deficiencies, including hypothyroidism. Hesx1 also acts as a transcriptional repressor of reporter gene constructs in tissue culture assays.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6560R-A555)
Fournisseur:
Bioss
Description:
The Oxysterol-binding protein (OSBP) family of proteins consist of OSBP (OSBP1) and OSBP2 (ORP-4), which share a high overall similarity. OSBPs are involved in lipid metabolism and signal transduction, as well as vesicle transport, and can translocate to the periphery of Golgi membranes when they are bound to oxysterols. The OSBP protein transports sterols from lysosomes to the nucleus, where sterols downregulate the genes for HMG synthetase, HMG-CoA reductase and the low density lipoprotein receptor (LDLR). OSBP localizes to the cytosol and is widely expressed, while OSBP2 is mainly detected in testis, retina and fetal liver. The extracellular signal-regulated kinase (ERK) signaling pathway is controlled by OSBP via its cholesterol-binding properties. OSBP binds with a high affinity to 25-hydroxy-cholesterol (25-HC), a suppressor of cholesterol synthesis gene transcription in cultured cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13597R-A555)
Fournisseur:
Bioss
Description:
The homeobox protein, HESX1, which is also known as Rathke’s pouch homeobox, HANF, homeodomain transcription factor, and anterior-restricted homeobox protein is a transcription factor that belongs to the homeodomain family of DNA binding proteins. HESX1 is initially expressed in embryonic stem cells and the primitive forebrain, and is essential for normal development of the eyes and other anterior CNS structures, such as the hypothalamus, the pituitary gland and the olfactory bulbs. The homeobox gene Hesx1 is expressed in the anterior visceral endoderm (AVE), anterior axial mesendoderm (AME), and anterior neural ectoderm (ANE) during early embryogenesis. Mutations in the Hesx1 gene are associated with disorders that are comparable with septo-optic dysplasia (SOD). These disorders are characterized by hypoplasia of the optic nerve, various types of forebrain defects and pituitary hormone deficiencies, including hypothyroidism. Hesx1 also acts as a transcriptional repressor of reporter gene constructs in tissue culture assays.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13597R-A488)
Fournisseur:
Bioss
Description:
The homeobox protein, HESX1, which is also known as Rathke’s pouch homeobox, HANF, homeodomain transcription factor, and anterior-restricted homeobox protein is a transcription factor that belongs to the homeodomain family of DNA binding proteins. HESX1 is initially expressed in embryonic stem cells and the primitive forebrain, and is essential for normal development of the eyes and other anterior CNS structures, such as the hypothalamus, the pituitary gland and the olfactory bulbs. The homeobox gene Hesx1 is expressed in the anterior visceral endoderm (AVE), anterior axial mesendoderm (AME), and anterior neural ectoderm (ANE) during early embryogenesis. Mutations in the Hesx1 gene are associated with disorders that are comparable with septo-optic dysplasia (SOD). These disorders are characterized by hypoplasia of the optic nerve, various types of forebrain defects and pituitary hormone deficiencies, including hypothyroidism. Hesx1 also acts as a transcriptional repressor of reporter gene constructs in tissue culture assays.
UOM:
1 * 100 µl
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